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Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH

Analyse Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C05
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.195
Source: MUS MUSCULUS
Molecule: Protein arginine N-methyltransferase 6
EC: 2.1.1.-, 2.1.1.125
UniProt: Q6NZB1
Ligands: SAH
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · resolution 2.195 · 1 distinct chain · 28% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arginine N-methyltransferase 6 (EC 2.1.1.-, 2.1.1.125)	protein	318	28% helix, 37% strand	Q6NZB1

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	335	0.62	0.79	40	SAH
2	70	0.56	0.88	17	empty

Compared structures

4C05 · Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with sah · the same entry in another collection · chain A against A, TM-score 1.00
Q6NZB1 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q6NZB1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6NZB1
Elsewhere: RCSB PDB 4C05 · PDBe 4C05 · UniProt Q6NZB1

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